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Interactive nmr and computer simulation studies of lanthionine‐ring structures
Author(s) -
Palmer D. E.,
Mierke D. F.,
Pattaroni C.,
Goodman M.,
Wakamiya T.,
Fukase K.,
Kitazawa M.,
Fujita H.,
Shiba T.
Publication year - 1989
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360280137
Subject(s) - lanthionine , chemistry , ring (chemistry) , nisin , molecule , lantibiotics , molecular dynamics , computational chemistry , stereochemistry , peptide , combinatorial chemistry , organic chemistry , biochemistry , antimicrobial
We report progress in elucidating the structure of nisin, a naturally occurring peptide antibiotic. Nisin contains five rings constrained by lanthionine or methyllanthionine bridges, as well as α,β‐unsaturated amino acids. We have determined conformations for two model compounds of ring A and a derivative of ring B through interactive nmr and computer simulation studies. High‐resolution nmr techniques provides structural information, which was further refined through molecular dynamics simulations. These methods are being applied to the remaining constrained fragments of the molecule. This conformational information will be employed in an aufbau approach to determining the structure of the entire molecule.